Adrenocortical nuclear progesterone-binding protein: Identification by photoaffinity labeling and evidence for deoxyribonucleic acid binding and stimulation by adrenocorticotropin
Abstract
Nuclei of the guinea pig adrenal cortex contain a protein that specifically binds progesterone and that, biochemically, is clearly distinct from the classical progesterone receptor. The adrenocortical nuclear progesterone-binding protein has now been purified more than 2000-fold by steroid-affinity chromatography with a 75% yield. The purified protein preparation demonstrated three major bands on sodium dodecyl sulfate-polyacrylamide gel of 79K, 74K, and 50K. To determine which of the three might represent the progesterone-binding protein, steroid photoaffinity labeling was performed which resulted in the specific and exclusive labeling of a 50K band. Thus, the adrenocortical nuclear progesterone-binding protein appears to be distinct from the classical progesterone receptor not only biochemically, but also on the basis of molecular size. To test whether the adrenocortical nuclear progesterone-binding protein can be hormonally stimulated, guinea pigs were treated with ACTH. The chronic administration of ACTH caused a 4- to 6-fold increase in the specific progesterone binding capacity without a change in the binding affinity. There appeared to be no significant difference in nuclear progesterone binding between the zona fasciculata and zona reticularis. This finding suggests a mediating role for the progesterone-binding protein in ACTH action. In addition, the nuclear progesterone-binding protein bound to nonspecific DNA sequences,more »
- Authors:
-
- National Institute of Child Health and Human Development, Bethesda, MD (USA)
- Publication Date:
- OSTI Identifier:
- 6215424
- Resource Type:
- Journal Article
- Journal Name:
- Endocrinology; (USA)
- Additional Journal Information:
- Journal Volume: 128:1; Journal ID: ISSN 0013-7227
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; DNA; BIOCHEMICAL REACTION KINETICS; PITUITARY HORMONES; PROGESTERONE; RECEPTORS; PROTEINS; LABELLING; ADRENAL GLANDS; AFFINITY; CELL NUCLEI; GUINEA PIGS; MOLECULAR WEIGHT; TRACER TECHNIQUES; TRITIUM COMPOUNDS; ANIMALS; BODY; CELL CONSTITUENTS; ENDOCRINE GLANDS; GLANDS; HORMONES; HYDROGEN COMPOUNDS; ISOTOPE APPLICATIONS; KETONES; KINETICS; MAMMALS; MEMBRANE PROTEINS; NUCLEIC ACIDS; ORGANIC COMPOUNDS; ORGANS; PEPTIDE HORMONES; PREGNANES; REACTION KINETICS; RODENTS; STEROID HORMONES; STEROIDS; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques
Citation Formats
Demura, T, Driscoll, W J, Lee, Y C, and Strott, C A. Adrenocortical nuclear progesterone-binding protein: Identification by photoaffinity labeling and evidence for deoxyribonucleic acid binding and stimulation by adrenocorticotropin. United States: N. p., 1991.
Web. doi:10.1210/endo-128-1-553.
Demura, T, Driscoll, W J, Lee, Y C, & Strott, C A. Adrenocortical nuclear progesterone-binding protein: Identification by photoaffinity labeling and evidence for deoxyribonucleic acid binding and stimulation by adrenocorticotropin. United States. https://doi.org/10.1210/endo-128-1-553
Demura, T, Driscoll, W J, Lee, Y C, and Strott, C A. 1991.
"Adrenocortical nuclear progesterone-binding protein: Identification by photoaffinity labeling and evidence for deoxyribonucleic acid binding and stimulation by adrenocorticotropin". United States. https://doi.org/10.1210/endo-128-1-553.
@article{osti_6215424,
title = {Adrenocortical nuclear progesterone-binding protein: Identification by photoaffinity labeling and evidence for deoxyribonucleic acid binding and stimulation by adrenocorticotropin},
author = {Demura, T and Driscoll, W J and Lee, Y C and Strott, C A},
abstractNote = {Nuclei of the guinea pig adrenal cortex contain a protein that specifically binds progesterone and that, biochemically, is clearly distinct from the classical progesterone receptor. The adrenocortical nuclear progesterone-binding protein has now been purified more than 2000-fold by steroid-affinity chromatography with a 75% yield. The purified protein preparation demonstrated three major bands on sodium dodecyl sulfate-polyacrylamide gel of 79K, 74K, and 50K. To determine which of the three might represent the progesterone-binding protein, steroid photoaffinity labeling was performed which resulted in the specific and exclusive labeling of a 50K band. Thus, the adrenocortical nuclear progesterone-binding protein appears to be distinct from the classical progesterone receptor not only biochemically, but also on the basis of molecular size. To test whether the adrenocortical nuclear progesterone-binding protein can be hormonally stimulated, guinea pigs were treated with ACTH. The chronic administration of ACTH caused a 4- to 6-fold increase in the specific progesterone binding capacity without a change in the binding affinity. There appeared to be no significant difference in nuclear progesterone binding between the zona fasciculata and zona reticularis. This finding suggests a mediating role for the progesterone-binding protein in ACTH action. In addition, the nuclear progesterone-binding protein bound to nonspecific DNA sequences, further suggesting a possible transcriptional regulatory role.},
doi = {10.1210/endo-128-1-553},
url = {https://www.osti.gov/biblio/6215424},
journal = {Endocrinology; (USA)},
issn = {0013-7227},
number = ,
volume = 128:1,
place = {United States},
year = {Tue Jan 01 00:00:00 EST 1991},
month = {Tue Jan 01 00:00:00 EST 1991}
}